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A1IA3_LOXHI
ID   A1IA3_LOXHI             Reviewed;         270 AA.
AC   C0JAQ9;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Dermonecrotic toxin LhSicTox-alphaIA2aiii {ECO:0000303|PubMed:19042943};
DE            EC=4.6.1.- {ECO:0000250|UniProtKB:Q4ZFU2};
DE   AltName: Full=Phospholipase D;
DE            Short=PLD;
DE   AltName: Full=Sphingomyelin phosphodiesterase D;
DE            Short=SMD;
DE            Short=SMase D;
DE            Short=Sphingomyelinase D;
DE   Flags: Fragment;
OS   Loxosceles hirsuta (Recluse spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX   NCBI_TaxID=571525;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RC   TISSUE=Venom gland;
RX   PubMed=19042943; DOI=10.1093/molbev/msn274;
RA   Binford G.J., Bodner M.R., Cordes M.H., Baldwin K.L., Rynerson M.R.,
RA   Burns S.N., Zobel-Thropp P.A.;
RT   "Molecular evolution, functional variation, and proposed nomenclature of
RT   the gene family that includes sphingomyelinase D in sicariid spider
RT   venoms.";
RL   Mol. Biol. Evol. 26:547-566(2009).
CC   -!- FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage
CC       between the phosphate and headgroup of certain phospholipids
CC       (sphingolipid and lysolipid substrates), forming an alcohol (often
CC       choline) and a cyclic phosphate (By similarity). This toxin acts on
CC       sphingomyelin (SM) (By similarity). It may also act on ceramide
CC       phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and
CC       lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine
CC       (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by
CC       transphosphatidylation, releasing exclusively cyclic phosphate products
CC       as second products (By similarity). Induces dermonecrosis, hemolysis,
CC       increased vascular permeability, edema, inflammatory response, and
CC       platelet aggregation (By similarity).
CC       {ECO:0000250|UniProtKB:A0A0D4WTV1, ECO:0000250|UniProtKB:P0CE80}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-
CC         1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892;
CC         Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-
CC         sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648,
CC         ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892;
CC         Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-
CC         2,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60700,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:58168, ChEBI:CHEBI:143947;
CC         Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-
CC         glycero-2,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60704,
CC         ChEBI:CHEBI:57603, ChEBI:CHEBI:64381, ChEBI:CHEBI:143947;
CC         Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8I914};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:19042943}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19042943}.
CC   -!- SIMILARITY: Belongs to the arthropod phospholipase D family. Class II
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The most common activity assay for dermonecrotic toxins
CC       detects enzymatic activity by monitoring choline release from
CC       substrate. Liberation of choline from sphingomyelin (SM) or
CC       lysophosphatidylcholine (LPC) is commonly assumed to result from
CC       substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or
CC       lysophosphatidic acid (LPA), respectively, as a second product.
CC       However, two studies from Lajoie and colleagues (2013 and 2015) report
CC       the observation of exclusive formation of cyclic phosphate products as
CC       second products, resulting from intramolecular transphosphatidylation.
CC       Cyclic phosphates have vastly different biological properties from
CC       their monoester counterparts, and they may be relevant to the pathology
CC       of brown spider envenomation. {ECO:0000250|UniProtKB:A0A0D4WTV1,
CC       ECO:0000250|UniProtKB:A0A0D4WV12, ECO:0000250|UniProtKB:Q4ZFU2}.
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DR   EMBL; FJ171344; ACN48840.1; -; mRNA.
DR   AlphaFoldDB; C0JAQ9; -.
DR   SMR; C0JAQ9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.190; -; 1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   SUPFAM; SSF51695; SSF51695; 1.
PE   2: Evidence at transcript level;
KW   Cytolysis; Dermonecrotic toxin; Disulfide bond; Hemolysis;
KW   Lipid degradation; Lipid metabolism; Lyase; Magnesium; Metal-binding;
KW   Secreted; Toxin.
FT   CHAIN           <1..270
FT                   /note="Dermonecrotic toxin LhSicTox-alphaIA2aiii"
FT                   /id="PRO_0000392751"
FT   ACT_SITE        2
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   ACT_SITE        38
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         24
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8I914"
FT   DISULFID        42..48
FT                   /evidence="ECO:0000250|UniProtKB:P0CE80"
FT   DISULFID        44..187
FT                   /evidence="ECO:0000250|UniProtKB:P0CE80"
FT   NON_TER         1
SQ   SEQUENCE   270 AA;  29988 MW;  E8B4580A3E62842C CRC64;
     GHMVNAIYQI DEFANLGANS IETDVSFDDN ANPEYTYHGI PCDCGRSCLK WENYNDFLKG
     LRSATTPGNS KYQSKLILVV FDLKTGSLYD NQASEAGKKL AKNLLKHYWN NGNNGGRAYI
     VLSIPDLNHY PLIKGFTDTL KQEGHPELLE KVGYDFSGND AVGDVAKAYK KAGVSGHVWQ
     SDGITNCLLR GLTRVKEAVA NRDSGNGYIN KVYYWTVDKR ATTRDALDAG VDGVMTNYPD
     VIADVMNEAA YKNKVRLATY EDSPWVTFKK
 
 
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